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Q6FI81 (CPIN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Anamorsin
Alternative name(s):
Cytokine-induced apoptosis inhibitor 1
Fe-S cluster assembly protein DRE2 homolog
Gene names
Name:CIAPIN1
ORF Names:CUA001, PRO0915
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length312 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has anti-apoptotic effects in the cell. Involved in negative control of cell death upon cytokine withdrawal. Promotes development of hematopoietic cells By similarity. Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis. Electrons are transferred to the Fe-S cluster from NADPH via the FAD- and FMN-containing protein NDOR1. Ref.17

Cofactor

Binds 1 2Fe-2S cluster per subunit. Ref.17 Ref.19

Subunit structure

Monomer. Interacts with NDOR1; its oxidized form can be reduced by NDOR1. Interacts with CHCHD4 and may be a substrate for CHCHD4 chaperone activity. Ref.17 Ref.19

Subcellular location

Cytoplasm. Nucleus. Mitochondrion. Mitochondrion intermembrane space Probable. Note: Imported into mitochondria (in vitro). Ref.10 Ref.19

Tissue specificity

Ubiquitously expressed. Highly expressed in heart, liver and pancreas. Ref.9

Domain

The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine (Ref.19). Ref.17 Ref.19

The C-terminal domain binds one 2Fe-2S iron-sulfur cluster but is otherwise mostly in an intrinsically disordered conformation. Ref.17 Ref.19

The twin Cx2C motifs are involved in the recognition by the mitochondrial CHCHD4/MIA40-GFER/ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space. Ref.17 Ref.19

Miscellaneous

'Ana-mors-in' means 'anti-death molecule' in Latin.

Sequence similarities

Belongs to the anamorsin family.

Sequence caution

The sequence AAC24312.1 differs from that shown. Reason: Erroneous gene model prediction.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

GLRX3O760033EBI-750511,EBI-374781

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q6FI81-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q6FI81-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q6FI81-3)

The sequence of this isoform differs from the canonical sequence as follows:
     53-66: SAHKESSFDIILSG → C

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 312312Anamorsin HAMAP-Rule MF_03115
PRO_0000079288

Regions

Region1 – 172172N-terminal domain HAMAP-Rule MF_03115
Region173 – 22351Linker HAMAP-Rule MF_03115
Region224 – 31289Intrinsically disordered HAMAP-Rule MF_03115
Motif274 – 2774Cx2C motif 1 HAMAP-Rule MF_03115
Motif285 – 2884Cx2C motif 2 HAMAP-Rule MF_03115

Sites

Metal binding2371Iron-sulfur (2Fe-2S)
Metal binding2461Iron-sulfur (2Fe-2S)
Metal binding2491Iron-sulfur (2Fe-2S)
Metal binding2511Iron-sulfur (2Fe-2S)

Amino acid modifications

Modified residue1821Phosphoserine Ref.13
Modified residue1831Phosphoserine Ref.13
Modified residue3051Phosphoserine Ref.14 Ref.16
Modified residue3071Phosphoserine Ref.12 Ref.14

Natural variations

Alternative sequence1 – 204204Missing in isoform 2.
VSP_012360
Alternative sequence53 – 6614SAHKE…IILSG → C in isoform 3.
VSP_012361
Natural variant341A → E.
Corresponds to variant rs11557672 [ dbSNP | Ensembl ].
VAR_033747
Natural variant521Q → E.
Corresponds to variant rs11557674 [ dbSNP | Ensembl ].
VAR_033748

Experimental info

Sequence conflict1421S → F in CAB66548. Ref.2
Sequence conflict1421S → F in CAG38576. Ref.4
Sequence conflict2781Y → C in CAG38576. Ref.4
Sequence conflict2891P → T in CAB66548. Ref.2
Sequence conflict2891P → T in CAG38576. Ref.4
Sequence conflict3101H → N in CAB66548. Ref.2
Sequence conflict3101H → N in CAG38576. Ref.4

Secondary structure

............................ 312
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 4, 2005. Version 2.
Checksum: 70A71D44074ABFBA

FASTA31233,582
        10         20         30         40         50         60 
MADFGISAGQ FVAVVWDKSS PVEALKGLVD KLQALTGNEG RVSVENIKQL LQSAHKESSF 

        70         80         90        100        110        120 
DIILSGLVPG STTLHSAEIL AEIARILRPG GCLFLKEPVE TAVDNNSKVK TASKLCSALT 

       130        140        150        160        170        180 
LSGLVEVKEL QREPLTPEEV QSVREHLGHE SDNLLFVQIT GKKPNFEVGS SRQLKLSITK 

       190        200        210        220        230        240 
KSSPSVKPAV DPAAAKLWTL SANDMEDDSM DLIDSDELLD PEDLKKPDPA SLRAASCGEG 

       250        260        270        280        290        300 
KKRKACKNCT CGLAEELEKE KSREQMSSQP KSACGNCYLG DAFRCASCPY LGMPAFKPGE 

       310 
KVLLSDSNLH DA 

« Hide

Isoform 2 [UniParc].

Checksum: C9B53F80FA24398A
Show »

FASTA10811,735
Isoform 3 [UniParc].

Checksum: 29CA61B57C265FE7
Show »

FASTA29932,213

References

« Hide 'large scale' references
[1]Yang Y., Xu X., Gao G., Xiao H., Chen Z., Han Z.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adrenal tumor.
[2]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Brain.
[3]"Gene expression profiling in human fetal liver and identification of tissue- and developmental-stage-specific genes through compiled expression profiles and efficient cloning of full-length cDNAs."
Yu Y., Zhang C., Zhou G., Wu S., Qu X., Wei H., Xing G., Dong C., Zhai Y., Wan J., Ouyang S., Li L., Zhang S., Zhou K., Zhang Y., Wu C., He F.
Genome Res. 11:1392-1403(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Fetal liver.
[4]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Testis.
[6]"Genome duplications and other features in 12 Mb of DNA sequence from human chromosome 16p and 16q."
Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J., Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X., Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C., Adams M.D.
Genomics 60:295-308(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain, Placenta, Skin and Testis.
[9]"Identification of a cytokine-induced antiapoptotic molecule anamorsin essential for definitive hematopoiesis."
Shibayama H., Takai E., Matsumura I., Kouno M., Morii E., Kitamura Y., Takeda J., Kanakura Y.
J. Exp. Med. 199:581-592(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Subcellular localization of CIAPIN1."
Hao Z., Li X., Qiao T., Du R., Zhang G., Fan D.
J. Histochem. Cytochem. 54:1437-1444(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Successful expression and purification of human CIAPIN1 in baculovirus-insect cell system and application of this system to investigation of its potential methyltransferase activity."
Hao Z., Li X., Qiao T., Fan D.
Int. J. Biol. Macromol. 42:27-32(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: LACK OF METHYLTRANSFERASE ACTIVITY.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-182 AND SER-183, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305 AND SER-307, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-305, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]"Molecular view of an electron transfer process essential for iron-sulfur protein biogenesis."
Banci L., Bertini I., Calderone V., Ciofi-Baffoni S., Giachetti A., Jaiswal D., Mikolajczyk M., Piccioli M., Winkelmann J.
Proc. Natl. Acad. Sci. U.S.A. 110:7136-7141(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NDOR1, DOMAIN, FUNCTION, COFACTOR.
[18]"Solution structure of the N-terminal domain in human cytokine-induced apoptosis inhibitor anamorsin."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 1-171.
[19]"Anamorsin is a [2Fe-2S] cluster-containing substrate of the Mia40-dependent mitochondrial protein trapping machinery."
Banci L., Bertini I., Ciofi-Baffoni S., Boscaro F., Chatzi A., Mikolajczyk M., Tokatlidis K., Winkelmann J.
Chem. Biol. 18:794-804(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-172, COFACTOR, INTERACTION WITH CHCHD4, SUBUNIT, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION, DOMAIN.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF248964 mRNA. Translation: AAG44562.1.
AL136613 mRNA. Translation: CAB66548.1.
AF116609 mRNA. Translation: AAF71034.1.
CR533545 mRNA. Translation: CAG38576.1.
AK292281 mRNA. Translation: BAF84970.1.
AC004382 Genomic DNA. Translation: AAC24311.1.
AC004382 Genomic DNA. Translation: AAC24312.1. Sequence problems.
CH471092 Genomic DNA. Translation: EAW82923.1.
BC002568 mRNA. Translation: AAH02568.1.
BC024196 mRNA. Translation: AAH24196.1.
BC067303 mRNA. Translation: AAH67303.1.
BC071740 mRNA. Translation: AAH71740.1.
CCDSCCDS10781.2. [Q6FI81-1]
RefSeqNP_064709.2. NM_020313.2. [Q6FI81-1]
XP_005256118.1. XM_005256061.2. [Q6FI81-3]
UniGeneHs.4900.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LD4NMR-A1-172[»]
2YUINMR-A1-170[»]
4M7RX-ray1.80A/B1-172[»]
ProteinModelPortalQ6FI81.
SMRQ6FI81. Positions 1-172.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121328. 17 interactions.
IntActQ6FI81. 4 interactions.
MINTMINT-1469842.
STRING9606.ENSP00000377914.

PTM databases

PhosphoSiteQ6FI81.

Polymorphism databases

DMDM57012667.

Proteomic databases

MaxQBQ6FI81.
PaxDbQ6FI81.
PRIDEQ6FI81.

Protocols and materials databases

DNASU57019.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394391; ENSP00000377914; ENSG00000005194. [Q6FI81-1]
ENST00000567518; ENSP00000456114; ENSG00000005194. [Q6FI81-3]
GeneID57019.
KEGGhsa:57019.
UCSCuc002ell.1. human. [Q6FI81-1]
uc002elm.1. human. [Q6FI81-3]

Organism-specific databases

CTD57019.
GeneCardsGC16M057462.
HGNCHGNC:28050. CIAPIN1.
HPAHPA041350.
HPA042182.
MIM608943. gene.
neXtProtNX_Q6FI81.
PharmGKBPA134978864.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5636.
HOGENOMHOG000241118.
HOVERGENHBG051104.
OMADSMDLID.
OrthoDBEOG7WHHC3.
PhylomeDBQ6FI81.
TreeFamTF314449.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ6FI81.
BgeeQ6FI81.
CleanExHS_CIAPIN1.
GenevestigatorQ6FI81.

Family and domain databases

Gene3D3.40.50.150. 1 hit.
HAMAPMF_03115. Anamorsin.
InterProIPR007785. Anamorsin.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PANTHERPTHR13273. PTHR13273. 1 hit.
PfamPF05093. CIAPIN1. 1 hit.
[Graphical view]
SUPFAMSSF53335. SSF53335. 1 hit.
ProtoNetSearch...

Other

ChiTaRSCIAPIN1. human.
EvolutionaryTraceQ6FI81.
GeneWikiCIAPIN1.
GenomeRNAi57019.
NextBio62770.
PROQ6FI81.
SOURCESearch...

Entry information

Entry nameCPIN1_HUMAN
AccessionPrimary (citable) accession number: Q6FI81
Secondary accession number(s): A8K8B6 expand/collapse secondary AC list , O75206, O75207, Q9H0W1, Q9P1L7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 4, 2005
Last sequence update: January 4, 2005
Last modified: July 9, 2014
This is version 97 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM